2qqs

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{{STRUCTURE_2qqs| PDB=2qqs | SCENE= }}
{{STRUCTURE_2qqs| PDB=2qqs | SCENE= }}
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'''JMJD2A tandem tudor domains in complex with a trimethylated histone H4-K20 peptide'''
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===JMJD2A tandem tudor domains in complex with a trimethylated histone H4-K20 peptide===
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==Overview==
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The lysine demethylase JMJD2A has the unique property of binding trimethylated peptides from two different histone sequences (H3K4me3 and H4K20me3) through its tudor domains. Here we show using X-ray crystallography and calorimetry that H3K4me3 and H4K20me3, which are recognized with similar affinities by JMJD2A, adopt radically different binding modes, to the extent that we were able to design single point mutations in JMJD2A that inhibited the recognition of H3K4me3 but not H4K20me3 and vice versa.
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{{ABSTRACT_PUBMED_18084306}}
==About this Structure==
==About this Structure==
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[[Category: Zinc]]
[[Category: Zinc]]
[[Category: Zinc-finger]]
[[Category: Zinc-finger]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 15:26:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:16:57 2008''

Revision as of 12:17, 29 July 2008

Image:2qqs.png

Template:STRUCTURE 2qqs

JMJD2A tandem tudor domains in complex with a trimethylated histone H4-K20 peptide

Template:ABSTRACT PUBMED 18084306

About this Structure

2QQS is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor., Lee J, Thompson JR, Botuyan MV, Mer G, Nat Struct Mol Biol. 2008 Jan;15(1):109-11. Epub 2007 Dec 16. PMID:18084306

Page seeded by OCA on Tue Jul 29 15:16:57 2008

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